|Ex λ||Em λ||EC (M-1 cm-1)||QY||Brightness||pKa||Maturation (min)||Lifetime (ns)|
|% Normal Cells||OSER/NE ratio||Cell Type||Reference|
|93.1 ± 2.1 (10000 cells)||-||HeLa||Cranfill et al. (2016)|
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mRuby was derived from eqFP611 with the following mutations: M12K/M15L/Y22H/D31E/V46I/K67R/H72Y/T73P/F102I/K120Q/T122R/L147M/S158T/Q159H/N163K/Y169H/E175V/E185G/F187I/F192I/F194A/K207N/H214R/C222A/D223G/P225_L231delinsGGG
In HEK293 cells expressing monomeric eqFP611 variants, the red fluorescence was not evenly distributed but rather appeared as dot-like structures in the cytoplasm... A similar effect was noticed for eqFP611 dimers that had the A/C interface disrupted. This result suggested that exposure of the A/C interface may have made a subcellular targeting signal accessible. Indeed, sequence analysis revealed that amino acids 229GRL231 at the C terminus, and also the preceding triplet 226SKL228 may serve as a type-1 peroxisomal targeting signal... We succeeded in removing peroxisomal targeting by replacing the C-terminal sequence 222CDLPSKLGRL231 of eqFP611 by 222AGLGGG227 [in mRuby]
Analysed by flow cytometry, the fluorescence signal of living HEK293 cells expressing the codon optimized variant [of mRuby] was 5–8 fold increased in comparison to the predecessor with unaltered codon usage but identical amino acid sequence.